› 3mwh

X-ray diffraction
2.05Å resolution

The 1.4 Ang crystal structure of the ArsD arsenic metallochaperone provides insights into its interactions with the ArsA ATPase

Released:
DOI: 10.2210/pdb3mwh/pdb
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Source organism: Escherichia coli
Primary publication:
The 1.4 A crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase.
Ye J, Ajees AA, Yang J, Rosen BP
Biochemistry 49 5206-12 (2010)
PMID: 20507177

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arsenical resistance operon trans-acting repressor ArsD Chains: A, B
Molecule details ›
Chains: A, B
Length: 110 amino acids
Theoretical weight: 12.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P46003 (Residues: 1-109; Coverage: 91%)
Gene name: arsD
Sequence domains: Arsenical resistance operon protein ArsD
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-D
Spacegroup: P21
Unit cell:
a: 37.676Å b: 74.223Å c: 40.83Å
α: 90° β: 97.77° γ: 90°
R-values:
R R work R free
0.274 0.271 0.324
Expression system: Escherichia coli

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Citations

1 review citation

Arsenic binding to proteins.
Shen et al. (2013)
11 other articles

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